Literature DB >> 8176370

Localization of the herpes simplex virus type 1 major capsid protein VP5 to the cell nucleus requires the abundant scaffolding protein VP22a.

P Nicholson1, C Addison, A M Cross, J Kennard, V G Preston, F J Rixon.   

Abstract

The intracellular distributions of three herpes simplex virus type 1 (HSV-1) capsid proteins, VP23, VP5 and VP22a, were examined using vaccinia virus and plasmid expression systems. During infection of cells with HSV-1 wild-type virus, all three proteins were predominantly located in the nucleus, which is the site of capsid assembly. However, when expressed in the absence of any other HSV-1 proteins, although VP22a was found exclusively in the nucleus as expected, VP5 and VP23 were distributed throughout the cell. Thus nuclear localization is not an intrinsic property of these proteins but must be mediated by one or more HSV-1-induced proteins. Co-expression experiments demonstrated that VP5 was efficiently transported to the nucleus in the presence of VP22a, but the distribution of VP23 was unaffected by the presence of either or both of the other two proteins.

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Year:  1994        PMID: 8176370     DOI: 10.1099/0022-1317-75-5-1091

Source DB:  PubMed          Journal:  J Gen Virol        ISSN: 0022-1317            Impact factor:   3.891


  48 in total

1.  Roles of triplex and scaffolding proteins in herpes simplex virus type 1 capsid formation suggested by structures of recombinant particles.

Authors:  A Saad; Z H Zhou; J Jakana; W Chiu; F J Rixon
Journal:  J Virol       Date:  1999-08       Impact factor: 5.103

2.  Cytoplasm-to-nucleus translocation of a herpesvirus tegument protein during cell division.

Authors:  G Elliott; P O'Hare
Journal:  J Virol       Date:  2000-03       Impact factor: 5.103

3.  Mutation of single hydrophobic residue I27, L35, F39, L58, L65, L67, or L71 in the N terminus of VP5 abolishes interaction with the scaffold protein and prevents closure of herpes simplex virus type 1 capsid shells.

Authors:  Jewell N Walters; Gerry L Sexton; J Michael McCaffery; Prashant Desai
Journal:  J Virol       Date:  2003-04       Impact factor: 5.103

4.  Sequential localization of two herpes simplex virus tegument proteins to punctate nuclear dots adjacent to ICP0 domains.

Authors:  Ian Hutchinson; Alison Whiteley; Helena Browne; Gillian Elliott
Journal:  J Virol       Date:  2002-10       Impact factor: 5.103

5.  A domain in the herpes simplex virus 1 triplex protein VP23 is essential for closure of capsid shells into icosahedral structures.

Authors:  Hong Seok Kim; Eugene Huang; Jigisha Desai; Marieta Sole; Erin N Pryce; Mercy E Okoye; Stanley Person; Prashant J Desai
Journal:  J Virol       Date:  2011-09-28       Impact factor: 5.103

6.  Analysis of HCF, the cellular cofactor of VP16, in herpes simplex virus-infected cells.

Authors:  S LaBoissière; P O'Hare
Journal:  J Virol       Date:  2000-01       Impact factor: 5.103

7.  Proline and tyrosine residues in scaffold proteins of herpes simplex virus 1 critical to the interaction with portal protein and its incorporation into capsids.

Authors:  Kui Yang; Joel D Baines
Journal:  J Virol       Date:  2009-05-27       Impact factor: 5.103

8.  Regions of the herpes simplex virus scaffolding protein that are important for intermolecular self-interaction.

Authors:  Valerie G Preston; Iris M McDougall
Journal:  J Virol       Date:  2002-01       Impact factor: 5.103

9.  Cytomegalovirus assembly protein precursor and proteinase precursor contain two nuclear localization signals that mediate their own nuclear translocation and that of the major capsid protein.

Authors:  S M Plafker; W Gibson
Journal:  J Virol       Date:  1998-10       Impact factor: 5.103

10.  Release of the catalytic domain N(o) from the herpes simplex virus type 1 protease is required for viral growth.

Authors:  L Matusick-Kumar; P J McCann; B J Robertson; W W Newcomb; J C Brown; M Gao
Journal:  J Virol       Date:  1995-11       Impact factor: 5.103

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